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A more recent version of this article appeared on March 1, 2003
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Submitted on June 25, 2002
Revised on September 30, 2002
Accepted on November 18, 2002
1 University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Department of Pharmacology, 675 Hoes Lane, Piscataway, NJ 08854
* Corresponding author. E-mail address: efimov{at}umdnj.edu.
The NUDF protein of the filamentous fungus Aspergillus nidulans functions in the cytoplasmic dynein pathway. It binds several proteins, including the NUDE protein. GFP-tagged NUDF and NUDA (dynein heavy chain) localize to linearly moving dashes ("comets") that coincide with microtubule ends. Herein, deletion of the nude gene did not eliminate the comets of NUDF and NUDA, but affected the behavior of NUDA. Comets were also observed with the GFP-tagged NUDE and its nonfunctional C-terminal domain. In addition, overexpressed NUDA and NUDE accumulated in specks that were either immobile or bounced randomly. Neither comets nor specks were observed with the functional N-terminal domain of NUDE, indicating that these structures are not essential for NUDE function. Furthermore, NUDF overproduction totally suppressed deletion of the nude gene. This implies that the function of NUDE is secondary to that of NUDF. Unexpectedly, NUDF overproduction inhibited one conditional nudA mutant and all tested apsA mutants. An allele-specific interaction between the nudF and nudA genes is consistent with a direct interaction between NUDF and dynein heavy chain. Since APSA and its yeast homolog Num1p are cortical proteins, an interaction between the nudF and apsA genes suggests a role for NUDF at the cell cortex.
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